Mark Paddock, Ph.D University of California, San Diego

• Paddock, M.L., Flores, M., Isaacson, R., Shepherd, J.N. and Okamura, M.Y. (2010) EPR and ENDOR investigation of rhodosemiquinone in bacterial reaction centers formed by B-branch electron transfer. Appl. Magn. Reson. 37, 39-48.
• Abresch, E.C., Gong, X-M., Paddock, M.L. and Okamura, M.Y. (2009) Electron Transfer from Cytochrome c2 to Reaction Center: A Transition State Model for Ionic Strength Effects due to Neutral Mutations. Biochemistry 48, 11390-11398
• Lin, S., Jaschke, P.R., Wang, H., Paddock, M., Tufts, A., Allen, J.P., Rosell, F.I., Mauk, A.G., Woodbury, N.W. and Beatty, J.T. (2009) Electron transfer in the Rhodobacter sphaeroides reaction center assembled with zinc bacteriochlorophyll. Proc Natl Acad Sci USA 106, 8537-8542
• Abresch, E.C., Paddock, M.L., Villalobos, M., Chang, C. and Okamura, M.Y. (2008) Interaction between Cytochrome c2 and the Photosynthetic Reaction Center from Rhodobacter sphaeroides: Role of Inter-Protein Hydrogen Bonds in Binding and Electron Transfer. Biochemistry 47, 13318-13325
• Paddock, M. L., Flores, M., Isaacson, R., Chang, C., Abresch, E. C. and Okamura, M. Y. (2007) ENDOR Spectroscopy Reveals Light Induced Movement of the H-Bond from Ser-L223 upon Forming the Semiquinone (QB- ) in Reaction Centers from Rhodobacter sphaeroides, Biochemistry 46, 8234-8243.
• Paddock, M. L., Isaacson, R. A., Abresch, E. C., and Okamura, M. Y. (2007) Light induced EPR spectra of reaction centers from Rhodobacter sphaeroides at 80K: Evidence for reduction of QB by B-branch electron transfer in native reaction centers, Appl Mag Reson 31, 1-15
• Paddock, M.L., Chang, C., Xu, Q., Abresch, E.C., Axelrod, H.L., Feher, G. and Okamura, M.Y. (2005) Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry 44, 6920-6928
• Xu, Q., Axelrod, H.L., Abresch, E.C., Paddock, M.L., Okamura, M.Y. and Feher, G. (2004) X-Ray Structure Determination of Three Mutants of the Bacterial Photosynthetic Reaction Centers from Rhodobacter sphaeroides: Altered Proton Transfer Pathways. Structure 12, 703-715
• Paddock, M.L., Feher, G. and Okamura, M.Y. (2003) Proton Transfer Pathways and Mechanism in Bacterial Reaction Centers. Febs Lett. 555, 45-50
• Paddock, M.L., Adelroth, P., Beatty, J.T., Feher, G. and Okamura, M.Y. (2002) Determination of Proton Transfer Rates by Chemical Rescue: Application to Bacterial Reaction Centers. Biochemistry 41, 14716-14725
• Adelroth, P., Paddock, M.L., Sagle, L.B., Feher, G. and Okamura, M.Y. (2000) Identification of the Proton Pathway in Bacterial Reaction Centers: Metal Ion Binding Decreases the Uptake Rate of Both Protons Associated with Reduction of Q_B to Q_BH₂ Share a Common Entry Point. Proc. Natl. Acad. Sci. USA 97, 13086-13091
• Paddock ML, Graige MS, Feher G, Okamura MY. (1999) Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn²⁺ or Cd²⁺. Proc Natl Acad Sci USA. 96, 6183-6188

MitoNEET:

• Zuris, J.A., Halim, D.A., Conlan, A.R., Abresch, E.C., Nechushtai, R., Paddock, M.L. and Jennings, P.A. (2010) Engineering the Redox Potential over a Wide Range within a New Class of FeS Proteins. J. Am. Chem. Soc. (Communication) 132, 13120-13122
• Dicus, M.M., Conlan, A., Nechushtai, R., Jennings, P.A., Paddock, M.L., Britt, R.D. and Stoll, S. (2010) The Binding of Histidine in the (Cys)3(His)1-coordinated [2Fe-2S] Cluster of Human mitoNEET. J. Am. Chem. Soc. 132, 2037-2049
• Bak, D.W., Zuris, J.A., Paddock, M.L., Jennings, P.A. and Elliott, S.J. (2009) Redox Characterization of the FeS Protein MitoNEET and Impact of Thiazolidinedione Drug Binding. Biochemistry 48, 10193-10195
• Conlan, A.R., Axelrod, H.L., Cohen, A.E., Abresch, E.C., Zuris, J., Yee, D., Nechushtai, R., Jennings, P. and Paddock, M.L. (2009) Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2. J Mol Biol. 392, 143-153
• Conlan, A., Paddock, M.L., Axelrod, H.L., Cohen, A.E., Abresch, E.C., Wiley, S., Roy, M., Nechushtai, R. and Jennings, P.A. (2009) The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain. Acta Crystallogr F 65, 654-659
• Tirrell, T.F., Paddock, M.L., Conlan, A., Smoll, E.J., Nechushtai, R., Jennings, P. and Kim, J. (2009) Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of mitoNEET: Comparison to the (Cys)4 mutant and implications of the pH effects on the labile metal center. Biochemistry 48, 4747-4752
• Paddock, M.L., Wiley, S.E., Axelrod, H.L., Cohen, A. E., Roy, M., Abresch, E. C., Capraro, D., Murphy, A. N., Nechushtai, R., Dixon, J.E. and Jennings, P.A. (2007) MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone, Proc. Natl. Acad. Sci. USA 104, 14342-14347
• Wiley, S.E., Paddock, M.L., Abresch, E. C., Gross, L., van der Geer, P., Nechushtai, R., Murphy, A. N., Jennings, P.A. and Dixon, J.E. (2007) The outer mitochondrial membrane protein mitoneet contains a novel redox active 2Fe-2S cluster. J. Biol. Chem 282, 23745-23749

Full list of publications available here.